The effect of rainbow trout plasma protein (RPP) on the gelation of Alaska pollock surimi was determined to evaluate the possibility of its commercialization as a new protein additive. For modori gel, the breaking force, deformation, whiteness, and water holding capacity increased as the addition amount of RPP (0 to 0.75 mg/g) increased, and decreased at higher concentration of RPP (0.75 to 1.50 mg/g) (P < 0.05). Protein solubility of modori gel in the mixture of SDS, urea, and beta-mercaptoethanol decreased as the addition amount of RPP increased up to 0.75 mg/g, and increased at higher concentration of RPP (0.75 to 1.50 mg/g) (P < 0.05). The contents of trichloroacetic acid-soluble peptide decreased as the addition amount of RPP (0 to 1.50 mg/g) increased (P < 0.05). Based on the result of sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), most myosin heavy chain of surimi was not degraded when RPP was added. Thus, RPP was supposed to act as a protease inhibitor in the gelation of Alaska pollock surimi. An RPP of 0.75 mg/g was the optimal concentration to prevent the gel weakening of Alaska pollock surimi. Compounds with molecular weights less than 10 kDa in RPP had no significant effect on the gelation of Alaska pollock surimi based on the result of the dialyzed RPP.
Recombinant chum salmon cystatin (RC) expressed in Saccharomyces cerevisiae was purified by His-select nickel affinity chromatography. The specific inhibitory activities of RC against papain and cathepsin L were 7.45 and 10.24 U/mg, respectively. RC was stable over pH 5.0 to 7.0 and at temperature below 65 degrees C. RC was used to prevent the gel weakening of Alaska pollock surimi. RC at 100 microg/g showed the highest inhibitory activity against the autolysis of surimi based on the analysis of TCA-soluble peptides. As the concentration of RC increased, both the breaking force and deformation of modori gel greatly increased (P < 0.05). The addition of RC resulted in less expressible drip, which coincided with the increase of whiteness. More myosin heavy chain (MHC) was retained as the addition of RC increased. Therefore, RC could prevent the degradation of proteins in Alaska pollock surimi and was better than egg white (EW). Thus, RC could be applied to Alaska pollock surimi to prevent gel weakening and RC at 100 microg/g was the optimal concentration.
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